In nature, amino acids are found in two forms, L and D enantiomers, except for glycine which
does not have a chiral center. The change of one form to the other will lead to a change in …

This tutorial review describes the principles and practices of electron capture and transfer
dissociation (ECD/ETD or ExD) mass spectrometry (MS) employed for peptide and protein …

For about three decades, the chemistry of cation radicals derived from organic molecules
had received a major impetus from mass spectrometry. This was because cation radicals …

Single cell analysis strives to probe molecular heterogeneity in morphologically similar cell
populations through quantitative or qualitative measurements of genetic, proteomic, or …

Deamidation of asparaginyl and isomerization of aspartyl residues in proteins proceed
through a succinimide intermediate producing a mixture of aspartyl and isoaspartyl residues …

A new two-dimensional ion mobility spectrometry approach combined with mass
spectrometry has been used to examine ubiquitin ions in the gas phase. In this approach …

Traditionally, the d-amino acid containing peptide (DAACP) candidate can be discovered by
observing the differences of biological activity and chromatographic retention time between …

Despite often minute concentrations in vivo, d-amino acid containing peptides (DAACPs) are
crucial to many life processes. Standard proteomics protocols fail to detect them as d/l …

A receptor binding class of d-amino acid-containing peptides (DAACPs) is formed in animals
from an enzymatically mediated post-translational modification of ribosomally translated all-l …

Ion− ion reactions between a variety of peptide cations (doubly and triply charged) and SO2
anions have been studied in a 3-D quadrupole ion trap, resulting in proton and electron …